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The binding constant, or affinity constant/association constant, is a special case of the equilibrium constant K, [1] and is the inverse of the dissociation constant. [2] It is associated with the binding and unbinding reaction of receptor (R) and ligand (L) molecules, which is formalized as: R + L ⇌ RL
Affinity describes how well a drug can bind to a receptor. Faster or stronger binding is represented by a higher affinity, or equivalently a lower dissociation constant. The EC 50 should not be confused with the affinity constant, K d. While the former reflects the drug concentration needed for a level of tissue response, the latter reflects ...
The PDBbind database is a comprehensive collection of experimentally measured binding affinity data (Kd, Ki, and IC50) for the protein-ligand complexes deposited in the Protein Data Bank (PDB). [ 1 ] [ 2 ] It thus provides a link between energetic and structural information of protein-ligand complexes, which is of great value to various studies ...
Many biological proteins and enzymes can possess more than one binding site. [3] Usually, when a ligand L binds with a macromolecule M, it can influence binding kinetics of other ligands L binding to the macromolecule. A simplified mechanism can be formulated if the affinity of all binding sites can be considered independent of the number of ...
IC 50 values are typically expressed as molar concentration. ... where K i is the binding affinity of the inhibitor, IC 50 is the functional strength of the inhibitor ...
The full sets of values within the ranges can be found in the Wiki code. (2) Binding affinities were determined via displacement studies in a variety of in-vitro systems with labeled estradiol and human ERα and ERβ proteins (except the ERβ values from Kuiper et al. (1997), which are rat ERβ).
The K i Database (or K i DB) is a public domain database of published binding affinities (K i) of drugs and chemical compounds for receptors, neurotransmitter transporters, ion channels, and enzymes. The resource is maintained by the University of North Carolina at Chapel Hill and is funded by the NIMH Psychoactive Drug Screening Program and by ...
In biochemistry, p 50 represents the partial pressure of a gas required to achieve 50% saturation of a particular protein's binding sites. [1] [2] Values of p 50 are negatively correlated with substrate affinity; lower values correspond to higher affinity and vice versa.